Journal
JOURNAL OF BIOMOLECULAR NMR
Volume 58, Issue 2, Pages 123-128Publisher
SPRINGER
DOI: 10.1007/s10858-013-9810-2
Keywords
Iron-sulfur proteins; Paramagnetic NMR; N-15-HSQC; Pulse sequences; Paramagnetic relaxation; Anamorsin
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Funding
- Programmi di Ricerca di Rilevante Interesse Nazionale (PRIN) [2009FAKHZT_001]
- POR CREO FESR [2007-20013]
- Ente Cassa di Risparmio di Firenze
- European Union ESFRI Instruct Core Centre Centro di Risonanze Magnetiche (Italy)
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A crucial factor for the understanding of structure-function relationships in metalloproteins is the identification of NMR signals from residues surrounding the metal cofactor. When the latter is paramagnetic, the NMR information in the proximity of the metal center may be scarce, because fast nuclear relaxation quenches signal intensity and coherence transfer efficiency. To identify residues at a short distance from a paramagnetic center, we developed a modified version of the N-15-HSQC experiment where (1) an inversion recovery filter is added prior to HSQC, (2) the INEPT period has been optimized according to fast relaxation of interested spins, (3) the inverse INEPT has been eliminated and signals acquired as antiphase doublets. The experiment has been successfully tested on a human [Fe2S2] protein which is involved in the biogenesis of iron-sulfur proteins. Thirteen H-N resonances, unobserved with conventional HSQC experiments, could be identified. The structural arrangement of the protein scaffold in the proximity of the Fe/S cluster is fundamental to comprehend the molecular processes responsible for the transfer of Fe/S groups in the iron-sulfur protein assembly machineries.
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